Department of Chemistry, University of Rome, Rome, Italy.
Biopolymers. 2009 Dec;91(12):1154-60. doi: 10.1002/bip.21215.
Gramicidin S (GS) analogues belong to an important class of cyclic peptides, characterized by an antiparallel double-stranded beta-sheet structure with Type II' beta-turns. Such compounds can be used as model systems to understand the folding/unfolding process of beta-hairpins and more in general of beta-structures. In the present study, we specifically investigate the folding/unfolding behavior of the hexameric Gramicidin S analogue GS6 by using all-atoms molecular dynamics (MD) simulations at different temperatures, coupled to a statistical mechanical model based on the Quasi Gaussian Entropy theory. Such an approach permits to describe the structural, thermodynamic, and kinetic properties of the peptide and to quantitatively characterize its folding/unfolding transitions.
短杆菌肽 S（GS）类似物属于一类重要的环肽，其特征是具有反平行双链β-折叠结构和 II'型β-转角。这些化合物可用作模型系统，以了解β发夹和更普遍的β结构的折叠/展开过程。在本研究中，我们特别通过使用全原子分子动力学（MD）模拟在不同温度下研究六聚体短杆菌肽 S 类似物 GS6 的折叠/展开行为，同时结合基于准高斯熵理论的统计力学模型。这种方法可以描述肽的结构、热力学和动力学性质，并定量表征其折叠/展开转变。
